ID A0A099J2T0_9MICO Unreviewed; 393 AA.
AC A0A099J2T0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Colicin V production protein {ECO:0000313|EMBL:KGJ71852.1};
DE SubName: Full=S1-C subfamily serine protease {ECO:0000313|EMBL:MBB5641415.1};
GN ORFNames=BJ997_001963 {ECO:0000313|EMBL:MBB5641415.1}, GY21_19385
GN {ECO:0000313|EMBL:KGJ71852.1};
OS Cryobacterium roopkundense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ71852.1, ECO:0000313|Proteomes:UP000029864};
RN [1] {ECO:0000313|EMBL:KGJ71852.1, ECO:0000313|Proteomes:UP000029864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ71852.1,
RC ECO:0000313|Proteomes:UP000029864};
RA Sisinthy S.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5641415.1, ECO:0000313|Proteomes:UP000561726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5641415.1,
RC ECO:0000313|Proteomes:UP000561726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGJ71852.1}.
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DR EMBL; JPXF01000123; KGJ71852.1; -; Genomic_DNA.
DR EMBL; JACHBQ010000001; MBB5641415.1; -; Genomic_DNA.
DR RefSeq; WP_035839944.1; NZ_JPXF01000123.1.
DR AlphaFoldDB; A0A099J2T0; -.
DR STRING; 1001240.GY21_19385; -.
DR MEROPS; S01.513; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9766361at2; -.
DR Proteomes; UP000029864; Unassembled WGS sequence.
DR Proteomes; UP000561726; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR003825; Colicin-V_CvpA.
DR InterPro; IPR047680; MarP-like.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; NF033740; MarP_fam_protase; 1.
DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR PANTHER; PTHR43019:SF36; SERINE PROTEASE RV3671C; 1.
DR Pfam; PF02674; Colicin_V; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:MBB5641415.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:MBB5641415.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029864};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 393 AA; 39206 MW; F75D7675614EC1B4 CRC64;
MTGSTVLDLF LIVLLLGSLV NGYRSGLVRS LSGIIGAIAG GIAAFFVVPL VGTWIPAPEW
RTPAALGAAV ILVAVGFSLG ASVGNSIGRV AHRSKLGIID RLLGAGFSAV ASALIASMVA
FSVGALGVPY LSPAIASSSV ISGIDNLTPD PVKSLLAQLR SAAVQEGLPR IVDAFSGPAP
ATADADTSSP ALAVAAQSVM RITGTAYACG QSQSGTGFVV APNRVITNAH VVAGVTEPVI
ESPAGEALPG TVVYFDSVND LAVIAVDGLE EPALPLGDDL SVGSSAVAHG YPFGGPFVAD
PARVLSLGTL SVADIYGQDP TPRQVYTLAS DVQQGESGGP LLSESGEVTG VIFAKSADTD
NVGYALALEE FAPVVAEAPG LTASVSSGTC IRG
//